ToF-SIMS analysis of amyloid beta aggregation on different lipid membranes

Biointerphases
Yuta YokoyamaHideo Iwai

Abstract

Amyloid beta (Aβ) peptides are considered to be strongly related to Alzheimer's disease. Aβ peptides form a β-sheet structure on hard lipid membranes and it would aggregate to form amyloid fibrils, which are toxic to cells. However, the aggregation mechanism of Aβ is not fully understood. To evaluate the influence of the lipid membrane condition for Aβ aggregation, the adsorption forms of Aβ (1-40) on mixture membranes of lipid 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) and cholesterol β-d-glucoside (β-CG) were investigated by time-of-flight secondary ion mass spectrometry. As a result, Aβ adsorbed along the localized DMPC lipid on the mixture lipid membranes, whereas it was adsorbed homogeneously on the pure DMPC and β-CG membranes. Moreover, amino acid fragments that mainly existed in the n-terminal of Aβ (1-40) peptide were strongly detected on the localized DMPC region. These results suggested that the Aβ was adsorbed along the localized DMPC lipid with a characteristic orientation. These findings suggest that the hardness of the membrane is very sensitive to coexisting materials and that surface hardness is important for aggregation of Aβ.

References

Mar 22, 2003·Biochimica Et Biophysica Acta·Diana Bach, Ellen Wachtel
Jun 23, 2011·Journal of Alzheimer's Disease : JAD·Francis HaneZoya Leonenko
Aug 16, 2012·Biointerphases·Daniel J Graham, David G Castner
Feb 15, 2014·Colloids and Surfaces. B, Biointerfaces·Toshinori ShimanouchiHiroshi Umakoshi
Feb 18, 2015·Analytical and Bioanalytical Chemistry·Satoka AoyagiHideo Iwai

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Citations

Oct 20, 2018·The Analyst·Lei YinJingkai Gu

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